scholarly journals Efficient generation of a monoclonal antibody against the human C-type lectin receptor DCIR by targeting murine dendritic cells

2010 ◽  
Vol 132 (1-2) ◽  
pp. 69-78 ◽  
Author(s):  
Gordon F. Heidkamp ◽  
Kirsten Neubert ◽  
Eric Haertel ◽  
Falk Nimmerjahn ◽  
Michel C. Nussenzweig ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Dendritic Cells ◽  
Lectin Receptor ◽  
Efficient Generation

scholarly journals Langerhans' cells, veiled cells, and interdigitating cells in the mouse recognized by a monoclonal antibody.

1986 ◽  
Vol 163 (4) ◽  
pp. 981-997 ◽  
Author(s):  
G Kraal ◽  
M Breel ◽  
M Janse ◽  
G Bruin
Keyword(s):  
Monoclonal Antibody ◽  
Bone Marrow ◽  
Dendritic Cells ◽  
Dendritic Cell ◽  
Langerhans Cells ◽  
Precursor Cells ◽  
Peritoneal Exudate ◽  
Peritoneal Exudate Cells ◽  
Interdigitating Cells

An mAb, NLDC-145, is described that specifically reacts with a group of nonlymphoid dendritic cells including Langerhans cells (LC), veiled cells (VC), and interdigitating cells (IDC). The antibody does not react with precursor cells in bone marrow and blood. Macrophages are not stained by the antibody, but a subpopulation of Ia+ peritoneal exudate cells is recognized. Possible relationships of the various nonlymphoid dendritic cell (NLDC) types are discussed.

scholarly journals C-Type Lectin Receptor Dectin-2 Binds to an Endogenous Protein β-Glucuronidase on Dendritic Cells

PLoS ONE ◽  
2017 ◽  
Vol 12 (1) ◽  
pp. e0169562 ◽  
Author(s):  
Daiki Mori ◽  
Kensuke Shibata ◽  
Sho Yamasaki
Keyword(s):  
Dendritic Cells ◽  
Lectin Receptor ◽  
Endogenous Protein

scholarly journals A single immunization with CAF08 provides newborns with Th1-mediated protection against Respiratory Syncytial Virus infection

2021 ◽  
Author(s):  
Simon van Haren ◽  
Gabriel Kristian Pedersen ◽  
Azad Kumar ◽  
Tracy Ruckwardt ◽  
Syed Moin ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Respiratory Syncytial Virus ◽  
Early Life ◽  
T Helper 1 ◽  
Newborn Mice ◽  
Cross Presentation ◽  
Lectin Receptor ◽  
Syncytial Virus ◽  
Human Dendritic Cells

Abstract Respiratory Syncytial Virus (RSV) is a leading cause of morbidity and mortality in children, due in part to their distinct immune system, characterized by impaired induction of T-helper 1 (Th1)-immunity. Here we describe cationic adjuvant formulation (CAF)-08, a liposomal vaccine formulation tailored to induce Th1 immunity in early life via synergistic engagement of Toll-like Receptor 7/8 and the C-type lectin receptor Mincle. Quantitative phosphoproteomics applied to human dendritic cells revealed a key role for Protein Kinase C-δ for enhanced Th1 cytokine production in neonatal dendritic cells and identified signaling events resulting in antigen cross-presentation. In vivo, a single immunization at birth with CAF08-adjuvanted RSV pre-fusion antigen protected newborn mice from RSV infection through induction of antigen-specific CD8+ and Th1 cells. Overall, we describe a novel pediatric adjuvant formulation and characterize its mechanism of action providing a promising avenue for development of early life vaccines against RSV and other intracellular pathogens.

CD209 (DC-SIGN) – role in the work of the innate immunity and pathogen penetration

2020 ◽  
Vol 1 (9) ◽  
pp. 64-71
Author(s):  
E. A. Klimov ◽  
◽  
E. K. Novitskaya ◽  
S. N. Koval’chuk ◽  
◽  
...  
Keyword(s):  
Immune Response ◽  
Innate Immunity ◽  
Dendritic Cells ◽  
Inflammatory Response ◽  
Signaling Pathway ◽  
Adhesion Molecule ◽  
Immune Evasion ◽  
Intercellular Adhesion Molecule ◽  
Lectin Receptor

Intercellular adhesion molecule CD209 (DC-SIGN) is a membrane C-type lectin receptor expressed on the surface of dendritic cells and macrophages. CD209 plays an important role in innate immunity. Many studies have shown the possibility of interaction of the CD209 molecule with a number of dangerous pathogens of humans and animals. This review summarizes information on the structure of the CD209 gene and its product, describes the role of the CD209 protein in the immune response, in the migration of dendritic cells from the blood to the tissue, and their interaction with neutrophils. The currently known signaling pathway of activation through the CD209 inflammatory response is presented. The role of CD209 as an endocytic antigen receptor and the participation of the protein in immune evasion of pathogens are discussed. The mechanisms known to date for the development of infections caused by pathogens of various nature in animals are described.

HIV gp120 receptors on human dendritic cells

Blood ◽  
2001 ◽  
Vol 98 (8) ◽  
pp. 2482-2488 ◽  
Author(s):  
Stuart G. Turville ◽  
Jim Arthos ◽  
Kelli Mac Donald ◽  
Garry Lynch ◽  
Hassan Naif ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Ex Vivo ◽  
Mannose Receptor ◽  
Lectin Receptor ◽  
Immunodeficiency Virus ◽  
Processing Pathways ◽  
Human Dendritic Cells ◽  
Hiv Gp120 ◽  
Hiv Envelope ◽  
Transfer Mechanisms

Abstract Dendritic cells (DCs) are important targets for human immunodeficiency virus (HIV) because of their roles during transmission and also maintenance of immune competence. Furthermore, DCs are a key cell in the development of HIV vaccines. In both these settings the mechanism of binding of the HIV envelope protein gp120 to DCs is of importance. Recently a single C-type lectin receptor (CLR), DC-SIGN, has been reported to be the predominant receptor on monocyte-derived DCs (MDDCs) rather than CD4. In this study a novel biotinylated gp120 assay was used to determine whether CLR or CD4 were predominant receptors on MDDCs and ex vivo blood DCs. CLR bound more than 80% of gp120 on MDDCs, with residual binding attributable to CD4, reconfirming that CLRs were the major receptors for gp120 on MDDCs. However, in contrast to recent reports, gp120 binding to at least 3 CLRs was observed: DC-SIGN, mannose receptor, and unidentified trypsin resistant CLR(s). In marked contrast, freshly isolated and cultured CD11c+ve and CD11c−ve blood DCs only bound gp120 via CD4. In view of these marked differences between MDDCs and blood DCs, HIV capture by DCs and transfer mechanisms to T cells as well as potential antigenic processing pathways will need to be determined for each DC phenotype.

scholarly journals The Human Monoclonal Antibody 3C12C, Targeting Activated Dendritic Cells Is a Potential New Immunosuppressive Agent

2015 ◽  
Vol 21 (2) ◽  
pp. S330-S331
Author(s):  
Nirupama D. Verma ◽  
David Munster ◽  
Therese Seldon ◽  
Yong Hua Sheng ◽  
Martina Jones ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Dendritic Cells ◽  
Human Monoclonal Antibody ◽  
Immunosuppressive Agent

scholarly journals Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners

2020 ◽  
Vol 295 (42) ◽  
pp. 14430-14444 ◽  
Author(s):  
Mariano Malamud ◽  
Gustavo J. Cavallero ◽  
Adriana C. Casabuono ◽  
Bernd Lepenies ◽  
María de los Ángeles Serradell ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Dendritic Cells ◽  
Protein Glycosylation ◽  
Immunomodulatory Activity ◽  
Glycosylation Pattern ◽  
Immunostimulatory Activity ◽  
Lectin Receptors ◽  
Lectin Receptor ◽  
Raw264.7 Macrophages ◽  
Lactobacillus Kefiri

S-layer (glyco)-proteins (SLPs) form a nanostructured envelope that covers the surface of different prokaryotes and show immunomodulatory activity. Previously, we have demonstrated that the S-layer glycoprotein from probiotic Lactobacillus kefiri CIDCA 8348 (SLP-8348) is recognized by Mincle (macrophage inducible C-type lectin receptor), and its adjuvanticity depends on the integrity of its glycans. However, the glycan's structure has not been described so far. Herein, we analyze the glycosylation pattern of three SLPs, SLP-8348, SLP-8321, and SLP-5818, and explore how these patterns impact their recognition by C-type lectin receptors and the immunomodulatory effect of the L. kefiri SLPs on antigen-presenting cells. High-performance anion-exchange chromatography–pulse amperometric detector performed after β-elimination showed glucose as the major component in the O-glycans of the three SLPs; however, some differences in the length of hexose chains were observed. No N-glycosylation signals were detected in SLP-8348 and SLP-8321, but SLP-5818 was observed to have two sites carrying complex N-glycans based on a site-specific analysis and a glycomic workflow of the permethylated glycans. SLP-8348 was previously shown to enhance LPS-induced activation on both RAW264.7 macrophages and murine bone marrow–derived dendritic cells; we now show that SLP-8321 and SLP-5818 have a similar effect regardless of the differences in their glycosylation patterns. Studies performed with bone marrow–derived dendritic cells from C-type lectin receptor–deficient mice revealed that the immunostimulatory activity of SLP-8321 depends on its recognition by Mincle, whereas SLP-5818's effects are dependent on SignR3 (murine ortholog of human DC-SIGN). These findings encourage further investigation of both the potential application of these SLPs as new adjuvants and the protein glycosylation mechanisms in these bacteria.

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